Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 4, Pages 1189-1194Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0610297104
Keywords
inititation complex; transcription; x-ray crystallography; protein-protein interaction
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Funding
- NIGMS NIH HHS [GM069769, R01 GM069769] Funding Source: Medline
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TFIID is an essential factor required for RNA polymerase 11 transcription but remains poorly understood because of its intrinsic complexity. Human TAF5, a 100-kDa subunit of general transcription factor TFIID, is an essential gene and plays a critical role in assembling the 1.2 MDa TFIID complex. We report here a structural analysis of the TAF5 protein. Our structure at 2.2-angstrom resolution of the TAF5-NTD2 domain reveals an alpha-helical domain with distant structural similarity to RNA polymerase II CTD interacting factors. The TAF5-NTD2 domain contains several conserved clefts likely to be critical for TFIID complex assembly. Our biochemical analysis of the human TAF5 protein demonstrates the ability of the N-terminal half of the TAF5 gene to form a flexible, extended dinner, a key property required for the assembly of the TFIID complex.
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